RANBP2 | ENSG00000153201 | NCBI 5903

Details for: RANBP2

Gene ID: 5903

Symbol: RANBP2

Ensembl ID: ENSG00000153201

Description: RAN binding protein 2

Associated with

Amplification of signal from the kinetochores
(R-HSA-141424)
Amplification of signal from unattached kinetochores via a mad2 inhibitory signal
(R-HSA-141444)
Antiviral mechanism by ifn-stimulated genes
(R-HSA-1169410)
Cell cycle
(R-HSA-1640170)
Cell cycle, mitotic
(R-HSA-69278)
Cell cycle checkpoints
(R-HSA-69620)
Cellular responses to stimuli
(R-HSA-8953897)
Cellular responses to stress
(R-HSA-2262752)
Cellular response to heat stress
(R-HSA-3371556)
Cytokine signaling in immune system
(R-HSA-1280215)
Defective tpr may confer susceptibility towards thyroid papillary carcinoma (tpc)
(R-HSA-5619107)
Disease
(R-HSA-1643685)
Diseases of signal transduction by growth factor receptors and second messengers
(R-HSA-5663202)
Disorders of transmembrane transporters
(R-HSA-5619115)
Eml4 and nudc in mitotic spindle formation
(R-HSA-9648025)
Export of viral ribonucleoproteins from nucleus
(R-HSA-168274)
Gene expression (transcription)
(R-HSA-74160)
Gene silencing by rna
(R-HSA-211000)
Glucose metabolism
(R-HSA-70326)
Glycolysis
(R-HSA-70171)
Hcmv early events
(R-HSA-9609690)
Hcmv infection
(R-HSA-9609646)
Hcmv late events
(R-HSA-9610379)
Hiv infection
(R-HSA-162906)
Hiv life cycle
(R-HSA-162587)
Host interactions of hiv factors
(R-HSA-162909)
Immune system
(R-HSA-168256)
Infectious disease
(R-HSA-5663205)
Influenza infection
(R-HSA-168255)
Influenza viral rna transcription and replication
(R-HSA-168273)
Interactions of rev with host cellular proteins
(R-HSA-177243)
Interactions of vpr with host cellular proteins
(R-HSA-176033)
Interferon signaling
(R-HSA-913531)
Isg15 antiviral mechanism
(R-HSA-1169408)
Late phase of hiv life cycle
(R-HSA-162599)
Metabolism
(R-HSA-1430728)
Metabolism of carbohydrates
(R-HSA-71387)
Metabolism of non-coding rna
(R-HSA-194441)
Metabolism of proteins
(R-HSA-392499)
Metabolism of rna
(R-HSA-8953854)
Mitotic anaphase
(R-HSA-68882)
Mitotic metaphase and anaphase
(R-HSA-2555396)
Mitotic prometaphase
(R-HSA-68877)
Mitotic prophase
(R-HSA-68875)
Mitotic spindle checkpoint
(R-HSA-69618)
M phase
(R-HSA-68886)
Nep/ns2 interacts with the cellular export machinery
(R-HSA-168333)
Ns1 mediated effects on host pathways
(R-HSA-168276)
Nuclear envelope breakdown
(R-HSA-2980766)
Nuclear import of rev protein
(R-HSA-180746)
Nuclear pore complex (npc) disassembly
(R-HSA-3301854)
Post-translational protein modification
(R-HSA-597592)
Processing of capped intron-containing pre-mrna
(R-HSA-72203)
Regulation of glucokinase by glucokinase regulatory protein
(R-HSA-170822)
Regulation of hsf1-mediated heat shock response
(R-HSA-3371453)
Resolution of sister chromatid cohesion
(R-HSA-2500257)
Rev-mediated nuclear export of hiv rna
(R-HSA-165054)
Rho gtpase effectors
(R-HSA-195258)
Rho gtpases activate formins
(R-HSA-5663220)
Sars-cov-2 activates/modulates innate and adaptive immune responses
(R-HSA-9705671)
Sars-cov-2 infection
(R-HSA-9694516)
Sars-cov-2-host interactions
(R-HSA-9705683)
Sars-cov infections
(R-HSA-9679506)
Separation of sister chromatids
(R-HSA-2467813)
Signaling by alk fusions and activated point mutants
(R-HSA-9725370)
Signaling by alk in cancer
(R-HSA-9700206)
Signaling by rho gtpases
(R-HSA-194315)
Signaling by rho gtpases, miro gtpases and rhobtb3
(R-HSA-9716542)
Signal transduction
(R-HSA-162582)
Slc transporter disorders
(R-HSA-5619102)
Snrnp assembly
(R-HSA-191859)
Sumo e3 ligases sumoylate target proteins
(R-HSA-3108232)
Sumoylation
(R-HSA-2990846)
Sumoylation of chromatin organization proteins
(R-HSA-4551638)
Sumoylation of dna damage response and repair proteins
(R-HSA-3108214)
Sumoylation of dna replication proteins
(R-HSA-4615885)
Sumoylation of rna binding proteins
(R-HSA-4570464)
Sumoylation of sumoylation proteins
(R-HSA-4085377)
Sumoylation of ubiquitinylation proteins
(R-HSA-3232142)
Transcriptional regulation by small rnas
(R-HSA-5578749)
Transport of mature mrna derived from an intron-containing transcript
(R-HSA-159236)
Transport of mature mrna derived from an intronless transcript
(R-HSA-159231)
Transport of mature mrnas derived from intronless transcripts
(R-HSA-159234)
Transport of mature transcript to cytoplasm
(R-HSA-72202)
Transport of ribonucleoproteins into the host nucleus
(R-HSA-168271)
Transport of the slbp dependant mature mrna
(R-HSA-159230)
Transport of the slbp independent mature mrna
(R-HSA-159227)
Trna processing
(R-HSA-72306)
Trna processing in the nucleus
(R-HSA-6784531)
Viral infection pathways
(R-HSA-9824446)
Viral messenger rna synthesis
(R-HSA-168325)
Vpr-mediated nuclear import of pics
(R-HSA-180910)
Gtpase activator activity
(GO:0005096)
Metal ion binding
(GO:0046872)
Peptidyl-prolyl cis-trans isomerase activity
(GO:0003755)
Protein-containing complex binding
(GO:0044877)
Protein binding
(GO:0005515)
Rna binding
(GO:0003723)
Small gtpase binding
(GO:0031267)
Sumo transferase activity
(GO:0019789)

Cells (max top 100)

(Cell Significance Index and respective Thresholds are uniquely calculated using our advanced thresholding algorithms to reveal cell-specific gene markers)

Cell Name: polychromatophilic erythroblast (CL0000550)
Fold Change: 380.1467
Cell Significance Index: -59.1300
Cell Name: hematopoietic oligopotent progenitor cell (CL0002032)
Fold Change: 230.5205
Cell Significance Index: -58.4700
Cell Name: embryonic stem cell (CL0002322)
Fold Change: 145.6253
Cell Significance Index: -59.9900
Cell Name: smooth muscle fiber of ileum (CL1000278)
Fold Change: 139.9001
Cell Significance Index: -66.0500
Cell Name: mucosal type mast cell (CL0000485)
Fold Change: 134.8899
Cell Significance Index: -54.8000
Cell Name: peripheral blood mononuclear cell (CL2000001)
Fold Change: 120.2892
Cell Significance Index: -61.8800
Cell Name: ileal goblet cell (CL1000326)
Fold Change: 98.5362
Cell Significance Index: -66.1200
Cell Name: ciliated cell of the bronchus (CL0002332)
Fold Change: 57.6805
Cell Significance Index: -55.0700
Cell Name: orthochromatic erythroblast (CL0000552)
Fold Change: 50.7561
Cell Significance Index: -62.5800
Cell Name: CD8-alpha-beta-positive, alpha-beta intraepithelial T cell (CL0000796)
Fold Change: 22.8717
Cell Significance Index: -61.2700
Cell Name: CD8-positive, alpha-beta regulatory T cell (CL0000795)
Fold Change: 17.1515
Cell Significance Index: -52.6800
Cell Name: stromal cell of bone marrow (CL0010001)
Fold Change: 16.0338
Cell Significance Index: -63.2700
Cell Name: epidermal Langerhans cell (CL0002457)
Fold Change: 11.0756
Cell Significance Index: -24.2400
Cell Name: L2/3-6 intratelencephalic projecting glutamatergic neuron (CL4023040)
Fold Change: 2.1176
Cell Significance Index: 424.7800
Cell Name: neoplastic cell (CL0001063)
Fold Change: 1.7129
Cell Significance Index: 339.9300
Cell Name: lung endothelial cell (CL1001567)
Fold Change: 1.6482
Cell Significance Index: 85.8500
Cell Name: tuft cell of colon (CL0009041)
Fold Change: 1.4108
Cell Significance Index: 1273.8600
Cell Name: pigmented epithelial cell (CL0000529)
Fold Change: 1.3964
Cell Significance Index: 2629.2100
Cell Name: non-pigmented ciliary epithelial cell (CL0002304)
Fold Change: 1.2782
Cell Significance Index: 811.8200
Cell Name: obsolete caudal ganglionic eminence derived GABAergic cortical interneuron (CL4023070)
Fold Change: 1.1793
Cell Significance Index: 423.0100
Cell Name: intermediate cell of urothelium (CL4030055)
Fold Change: 1.1595
Cell Significance Index: 209.0300
Cell Name: basal cell of urothelium (CL1000486)
Fold Change: 1.0730
Cell Significance Index: 131.9400
Cell Name: cell in vitro (CL0001034)
Fold Change: 0.9227
Cell Significance Index: 503.9200
Cell Name: intestinal crypt stem cell of colon (CL0009043)
Fold Change: 0.8759
Cell Significance Index: 95.2700
Cell Name: GABAergic interneuron (CL0011005)
Fold Change: 0.8577
Cell Significance Index: 593.2200
Cell Name: tonsil germinal center B cell (CL2000006)
Fold Change: 0.8493
Cell Significance Index: 100.1600
Cell Name: cardiac muscle myoblast (CL0000513)
Fold Change: 0.7185
Cell Significance Index: 55.1400
Cell Name: stromal cell of ovary (CL0002132)
Fold Change: 0.6729
Cell Significance Index: 92.4100
Cell Name: basal cell of prostate epithelium (CL0002341)
Fold Change: 0.6481
Cell Significance Index: 17.6400
Cell Name: acinar cell of salivary gland (CL0002623)
Fold Change: 0.6136
Cell Significance Index: 28.6100
Cell Name: enterocyte of epithelium of small intestine (CL1000334)
Fold Change: 0.5942
Cell Significance Index: 17.1200
Cell Name: luminal adaptive secretory precursor cell of mammary gland (CL4033057)
Fold Change: 0.5830
Cell Significance Index: 27.4000
Cell Name: indirect pathway medium spiny neuron (CL4023029)
Fold Change: 0.5299
Cell Significance Index: 23.4400
Cell Name: retinal progenitor cell (CL0002672)
Fold Change: 0.5002
Cell Significance Index: 28.0700
Cell Name: hair follicular keratinocyte (CL2000092)
Fold Change: 0.4397
Cell Significance Index: 194.4000
Cell Name: skeletal muscle fiber (CL0008002)
Fold Change: 0.3871
Cell Significance Index: 9.9500
Cell Name: enteroendocrine cell of colon (CL0009042)
Fold Change: 0.3637
Cell Significance Index: 69.2100
Cell Name: hippocampal granule cell (CL0001033)
Fold Change: 0.2893
Cell Significance Index: 19.4500
Cell Name: direct pathway medium spiny neuron (CL4023026)
Fold Change: 0.2849
Cell Significance Index: 10.7900
Cell Name: basal epithelial cell of tracheobronchial tree (CL0002329)
Fold Change: 0.2650
Cell Significance Index: 7.4100
Cell Name: lens epithelial cell (CL0002224)
Fold Change: 0.2581
Cell Significance Index: 397.4100
Cell Name: pancreatic acinar cell (CL0002064)
Fold Change: 0.2426
Cell Significance Index: 41.4200
Cell Name: fibroblast of mammary gland (CL0002555)
Fold Change: 0.2177
Cell Significance Index: 6.2400
Cell Name: cortical cell of adrenal gland (CL0002097)
Fold Change: 0.2161
Cell Significance Index: 5.7900
Cell Name: anterior lens cell (CL0002223)
Fold Change: 0.2067
Cell Significance Index: 381.2200
Cell Name: ciliary muscle cell (CL1000443)
Fold Change: 0.1939
Cell Significance Index: 88.0100
Cell Name: epithelial cell of small intestine (CL0002254)
Fold Change: 0.1125
Cell Significance Index: 18.3000
Cell Name: colon goblet cell (CL0009039)
Fold Change: 0.0563
Cell Significance Index: 5.5700
Cell Name: sebum secreting cell (CL0000317)
Fold Change: 0.0556
Cell Significance Index: 3.9300
Cell Name: odontoblast (CL0000060)
Fold Change: 0.0442
Cell Significance Index: 5.6600
Cell Name: secondary lens fiber (CL0002225)
Fold Change: 0.0107
Cell Significance Index: 14.4900
Cell Name: placental villous trophoblast (CL2000060)
Fold Change: 0.0007
Cell Significance Index: 0.0200
Cell Name: kidney loop of Henle cortical thick ascending limb epithelial cell (CL1001109)
Fold Change: -0.0062
Cell Significance Index: -4.5200
Cell Name: pancreatic A cell (CL0000171)
Fold Change: -0.0338
Cell Significance Index: -25.0100
Cell Name: gut absorptive cell (CL0000677)
Fold Change: -0.0495
Cell Significance Index: -2.9700
Cell Name: pulmonary alveolar epithelial cell (CL0000322)
Fold Change: -0.0502
Cell Significance Index: -37.9800
Cell Name: pancreatic PP cell (CL0002275)
Fold Change: -0.0579
Cell Significance Index: -36.1800
Cell Name: type B pancreatic cell (CL0000169)
Fold Change: -0.0903
Cell Significance Index: -50.9500
Cell Name: eye photoreceptor cell (CL0000287)
Fold Change: -0.1047
Cell Significance Index: -6.6000
Cell Name: forebrain neuroblast (CL1000042)
Fold Change: -0.1100
Cell Significance Index: -6.7600
Cell Name: lactocyte (CL0002325)
Fold Change: -0.1163
Cell Significance Index: -15.0300
Cell Name: abnormal cell (CL0001061)
Fold Change: -0.1268
Cell Significance Index: -12.9500
Cell Name: intestinal crypt stem cell of small intestine (CL0009017)
Fold Change: -0.1338
Cell Significance Index: -2.8500
Cell Name: pancreatic D cell (CL0000173)
Fold Change: -0.1551
Cell Significance Index: -32.6700
Cell Name: early pro-B cell (CL0002046)
Fold Change: -0.1568
Cell Significance Index: -10.1200
Cell Name: bladder urothelial cell (CL1001428)
Fold Change: -0.1779
Cell Significance Index: -9.2400
Cell Name: pigmented ciliary epithelial cell (CL0002303)
Fold Change: -0.1849
Cell Significance Index: -26.8800
Cell Name: dopaminergic neuron (CL0000700)
Fold Change: -0.1997
Cell Significance Index: -57.4500
Cell Name: enterocyte of epithelium of large intestine (CL0002071)
Fold Change: -0.2186
Cell Significance Index: -9.9100
Cell Name: pancreatic endocrine cell (CL0008024)
Fold Change: -0.2704
Cell Significance Index: -30.8700
Cell Name: pancreatic ductal cell (CL0002079)
Fold Change: -0.2927
Cell Significance Index: -33.5300
Cell Name: epithelial cell of stomach (CL0002178)
Fold Change: -0.3295
Cell Significance Index: -38.4000
Cell Name: progenitor cell of mammary luminal epithelium (CL0009116)
Fold Change: -0.3392
Cell Significance Index: -25.2800
Cell Name: hippocampal pyramidal neuron (CL1001571)
Fold Change: -0.3494
Cell Significance Index: -9.9700
Cell Name: Hofbauer cell (CL3000001)
Fold Change: -0.3544
Cell Significance Index: -2.8900
Cell Name: cerebellar granule cell (CL0001031)
Fold Change: -0.3577
Cell Significance Index: -6.1300
Cell Name: retinal rod cell (CL0000604)
Fold Change: -0.4094
Cell Significance Index: -4.8800
Cell Name: smooth muscle cell of sphincter of pupil (CL0002243)
Fold Change: -0.4207
Cell Significance Index: -43.8100
Cell Name: GABAergic amacrine cell (CL4030027)
Fold Change: -0.5184
Cell Significance Index: -6.4300
Cell Name: peg cell (CL4033014)
Fold Change: -0.5434
Cell Significance Index: -12.5600
Cell Name: transit amplifying cell of small intestine (CL0009012)
Fold Change: -0.5491
Cell Significance Index: -11.3900
Cell Name: granulosa cell (CL0000501)
Fold Change: -0.5528
Cell Significance Index: -14.5400
Cell Name: neutrophil progenitor cell (CL0000834)
Fold Change: -0.5744
Cell Significance Index: -15.3700
Cell Name: kidney loop of Henle descending limb epithelial cell (CL1001021)
Fold Change: -0.6712
Cell Significance Index: -53.1600
Cell Name: glycinergic neuron (CL1001509)
Fold Change: -0.7062
Cell Significance Index: -37.0800
Cell Name: type I muscle cell (CL0002211)
Fold Change: -0.8570
Cell Significance Index: -20.9100
Cell Name: centrilobular region hepatocyte (CL0019029)
Fold Change: -0.8721
Cell Significance Index: -14.6900
Cell Name: intestinal tuft cell (CL0019032)
Fold Change: -0.8814
Cell Significance Index: -54.0400
Cell Name: transit amplifying cell of colon (CL0009011)
Fold Change: -0.9388
Cell Significance Index: -30.0700
Cell Name: conjunctival epithelial cell (CL1000432)
Fold Change: -0.9843
Cell Significance Index: -13.4300
Cell Name: CD4-positive, alpha-beta memory T cell, CD45RO-positive (CL0001204)
Fold Change: -1.0480
Cell Significance Index: -30.7800
Cell Name: endothelial cell of placenta (CL0009092)
Fold Change: -1.1073
Cell Significance Index: -6.6900
Cell Name: mesenchymal cell (CL0008019)
Fold Change: -1.1162
Cell Significance Index: -18.6800
Cell Name: cardiac muscle cell (CL0000746)
Fold Change: -1.1190
Cell Significance Index: -16.5200
Cell Name: fibro/adipogenic progenitor cell (CL0009099)
Fold Change: -1.1190
Cell Significance Index: -56.5500
Cell Name: CD14-positive, CD16-negative classical monocyte (CL0002057)
Fold Change: -1.1194
Cell Significance Index: -20.6900
Cell Name: mesonephric nephron tubule epithelial cell (CL1000022)
Fold Change: -1.1200
Cell Significance Index: -38.9200
Cell Name: decidual cell (CL2000002)
Fold Change: -1.1325
Cell Significance Index: -18.1700
Cell Name: cortical interneuron (CL0008031)
Fold Change: -1.1379
Cell Significance Index: -27.2900
Cell Name: cardiac endothelial cell (CL0010008)
Fold Change: -1.1660
Cell Significance Index: -16.7700

Cell ID: Standard Cell Ontology term used for mapping and comparing cells across experiments. Ensures consistency in analyzing cellular functions across tissues.
Fold Change: Represents the ratio of the current Cell Significance Index to the Cell Significance Index Threshold, indicating how much the gene expression has changed compared to a baseline.
Cell Significance Index: Reflects how strongly a gene is expressed in this specific cell.

**Key Characteristics** RANBP2 is a member of the SUMOylation system, which is a post-translational modification process that involves the covalent attachment of small ubiquitin-like modifier (SUMO) proteins to target proteins. As an E3 SUMO-protein ligase, RANBP2 recognizes and binds to specific motifs on target proteins, facilitating the transfer of SUMO molecules. RANBP2 is characterized by its ability to recognize and bind to specific SUMOylation motifs, which are often located near the N-terminus or C-terminus of target proteins. RANBP2 is also involved in various signaling pathways, including the regulation of cell cycle progression, apoptosis, and immune responses. Its expression is highly regulated, with significant fluctuations in response to cellular stress, growth factors, and viral infections. **Pathways and Functions** RANBP2 is involved in numerous signaling pathways, including: 1. **Cell cycle regulation**: RANBP2 regulates the cell cycle by modulating the activity of key proteins involved in DNA replication, repair, and cell division. 2. **Apoptosis**: RANBP2 modulates apoptosis by regulating the activity of pro-apoptotic and anti-apoptotic proteins. 3. **Immune responses**: RANBP2 regulates immune responses by modulating the activity of immune cells, including T cells and dendritic cells. 4. **Gene expression**: RANBP2 regulates gene expression by modulating the activity of transcription factors and chromatin remodeling complexes. 5. **Viral infections**: RANBP2 regulates viral infections by modulating the activity of viral proteins and host immune responses. **Clinical Significance** Dysregulation of RANBP2 has been implicated in several diseases, including: 1. **Cancer**: RANBP2 is overexpressed in various types of cancer, including breast, lung, and colon cancer, and is associated with poor prognosis. 2. **Viral infections**: RANBP2 is involved in the regulation of viral infections, including HIV, HCMV, and SARS-CoV-2. 3. **Autoimmune disorders**: RANBP2 is involved in the regulation of autoimmune responses, including rheumatoid arthritis and lupus. 4. **Neurological disorders**: RANBP2 is involved in the regulation of neurological disorders, including Alzheimer's disease and Parkinson's disease. In summary, RANBP2 is a critical protein that plays a central role in various cellular processes, including signal transduction, gene expression, and cell cycle regulation. Its dysregulation has been implicated in several diseases, including cancer, viral infections, and autoimmune disorders. Further research is needed to fully understand the mechanisms by which RANBP2 regulates cellular processes and to develop therapeutic strategies for the treatment of diseases associated with RANBP2 dysregulation.

Disclaimer: This summary is generated by an AI language model and may contain inaccuracies or hallucinations. However, it is cross-referenced with curated gene expression data from major biological sources. Please verify the information before use.

E3 SUMO-protein ligase RanBP2

Genular Protein ID: 689873332

Symbol: RBP2_HUMAN

Name: E3 SUMO-protein ligase RanBP2

UniProtKB Accession Codes:

P49792 Q13074 Q15280 Q53TE2 Q59FH7

Database IDs:

Citations:

PubMed ID: 7775481

Title: Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region.

PubMed ID: 7775481

DOI: 10.1074/jbc.270.23.14209

PubMed ID: 7603572

Title: A giant nucleopore protein that binds Ran/TC4.

PubMed ID: 7603572

DOI: 10.1038/376184a0

PubMed ID: 15815621

Title: Generation and annotation of the DNA sequences of human chromosomes 2 and 4.

PubMed ID: 15815621

DOI: 10.1038/nature03466

PubMed ID: 7724562

Title: The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif.

PubMed ID: 7724562

DOI: 10.1073/pnas.92.8.3328

PubMed ID: 11792325

Title: The nucleoporin RanBP2 has SUMO1 E3 ligase activity.

PubMed ID: 11792325

DOI: 10.1016/s0092-8674(01)00633-x

PubMed ID: 12032081

Title: The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase.

PubMed ID: 12032081

DOI: 10.1093/emboj/21.11.2682

PubMed ID: 11839768

Title: Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export.

PubMed ID: 11839768

DOI: 10.1083/jcb.200106046

PubMed ID: 15144186

Title: Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry.

PubMed ID: 15144186

DOI: 10.1021/ac035352d

PubMed ID: 14729961

Title: RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the nuclear pore complex and functions in nuclear mRNA export.

PubMed ID: 14729961

DOI: 10.1128/mcb.24.3.1155-1167.2004

PubMed ID: 15378033

Title: The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type.

PubMed ID: 15378033

DOI: 10.1038/nsmb834

PubMed ID: 15388847

Title: Identification of a SUMO-binding motif that recognizes SUMO-modified proteins.

PubMed ID: 15388847

DOI: 10.1073/pnas.0403498101

PubMed ID: 15608651

Title: Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection.

PubMed ID: 15608651

DOI: 10.1038/nsmb878

PubMed ID: 16620772

Title: A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers.

PubMed ID: 16620772

DOI: 10.1016/j.abb.2006.03.002

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16332688

Title: Parkin ubiquitinates and promotes the degradation of RanBP2.

PubMed ID: 16332688

DOI: 10.1074/jbc.m504994200

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 18220336

Title: Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis.

PubMed ID: 18220336

DOI: 10.1021/pr0705441

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 18318008

Title: Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography.

PubMed ID: 18318008

DOI: 10.1002/pmic.200700884

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 18946085

Title: RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin.

PubMed ID: 18946085

DOI: 10.1091/mbc.e08-05-0511

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20005110

Title: mRNA export from mammalian cell nuclei is dependent on GANP.

PubMed ID: 20005110

DOI: 10.1016/j.cub.2009.10.078

PubMed ID: 20386726

Title: Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes and regulate centrosome and nuclear positioning during mitotic entry.

PubMed ID: 20386726

DOI: 10.1371/journal.pbio.1000350

PubMed ID: 20676357

Title: Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases.

PubMed ID: 20676357

DOI: 10.1371/journal.pbio.1000439

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22902403

Title: The oncogene eIF4E reprograms the nuclear pore complex to promote mRNA export and oncogenic transformation.

PubMed ID: 22902403

DOI: 10.1016/j.celrep.2012.07.007

PubMed ID: 22155184

Title: Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells.

PubMed ID: 22155184

DOI: 10.1053/j.gastro.2011.11.041

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 25218447

Title: Uncovering global SUMOylation signaling networks in a site-specific manner.

PubMed ID: 25218447

DOI: 10.1038/nsmb.2890

PubMed ID: 25114211

Title: Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli.

PubMed ID: 25114211

DOI: 10.1073/pnas.1413825111

PubMed ID: 25772364

Title: SUMO-2 orchestrates chromatin modifiers in response to DNA damage.

PubMed ID: 25772364

DOI: 10.1016/j.celrep.2015.02.033

PubMed ID: 25755297

Title: System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability.

PubMed ID: 25755297

DOI: 10.1074/mcp.o114.044792

PubMed ID: 28112733

Title: Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation.

PubMed ID: 28112733

DOI: 10.1038/nsmb.3366

PubMed ID: 32690953

Title: Vpu modulates DNA repair to suppress innate sensing and hyper-integration of HIV-1.

PubMed ID: 32690953

DOI: 10.1038/s41564-020-0753-6

PubMed ID: 10078529

Title: Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport.

PubMed ID: 10078529

DOI: 10.1038/17969

PubMed ID: 15826666

Title: Solution structure of the Ran-binding domain 2 of RanBP2 and its interaction with the C terminus of Ran.

PubMed ID: 15826666

DOI: 10.1016/j.jmb.2005.02.033

PubMed ID: 15931224

Title: Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex.

PubMed ID: 15931224

DOI: 10.1038/nature03588

PubMed ID: 22194619

Title: Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2.

PubMed ID: 22194619

DOI: 10.1074/jbc.m111.321141

PubMed ID: 22959972

Title: Crystal structure of the N-terminal domain of Nup358/RanBP2.

PubMed ID: 22959972

DOI: 10.1016/j.jmb.2012.08.026

PubMed ID: 23353830

Title: Structural and functional analysis of the C-terminal domain of Nup358/RanBP2.

PubMed ID: 23353830

DOI: 10.1016/j.jmb.2013.01.021

PubMed ID: 19118815

Title: Infection-triggered familial or recurrent cases of acute necrotizing encephalopathy caused by mutations in a component of the nuclear pore, RANBP2.

PubMed ID: 19118815

DOI: 10.1016/j.ajhg.2008.12.009

PubMed ID: 23041776

Title: A translocation t(2;8)(q12;p11) fuses FGFR1 to a novel partner gene, RANBP2/NUP358, in a myeloproliferative/myelodysplastic neoplasm.

PubMed ID: 23041776

DOI: 10.1038/leu.2012.286

PubMed ID: 34400285

Title: RANBP2 mutation causing autosomal dominant acute necrotizing encephalopathy attenuates its interaction with COX11.

PubMed ID: 34400285

DOI: 10.1016/j.neulet.2021.136173

Sequence Information:

Length: 3224
Mass: 358199
Checksum: 4CD9A3D5E77183FB
Sequence:

MRRSKADVER YIASVQGSTP SPRQKSMKGF YFAKLYYEAK EYDLAKKYIC TYINVQERDP 
KAHRFLGLLY ELEENTDKAV ECYRRSVELN PTQKDLVLKI AELLCKNDVT DGRAKYWLER 
AAKLFPGSPA IYKLKEQLLD CEGEDGWNKL FDLIQSELYV RPDDVHVNIR LVEVYRSTKR 
LKDAVAHCHE AERNIALRSS LEWNSCVVQT LKEYLESLQC LESDKSDWRA TNTDLLLAYA 
NLMLLTLSTR DVQESRELLQ SFDSALQSVK SLGGNDELSA TFLEMKGHFY MHAGSLLLKM 
GQHSSNVQWR ALSELAALCY LIAFQVPRPK IKLIKGEAGQ NLLEMMACDR LSQSGHMLLN 
LSRGKQDFLK EIVETFANKS GQSALYDALF SSQSPKDTSF LGSDDIGNID VREPELEDLT 
RYDVGAIRAH NGSLQHLTWL GLQWNSLPAL PGIRKWLKQL FHHLPHETSR LETNAPESIC 
ILDLEVFLLG VVYTSHLQLK EKCNSHHSSY QPLCLPLPVC KQLCTERQKS WWDAVCTLIH 
RKAVPGNVAK LRLLVQHEIN TLRAQEKHGL QPALLVHWAE CLQKTGSGLN SFYDQREYIG 
RSVHYWKKVL PLLKIIKKKN SIPEPIDPLF KHFHSVDIQA SEIVEYEEDA HITFAILDAV 
NGNIEDAVTA FESIKSVVSY WNLALIFHRK AEDIENDALS PEEQEECKNY LRKTRDYLIK 
IIDDSDSNLS VVKKLPVPLE SVKEMLNSVM QELEDYSEGG PLYKNGSLRN ADSEIKHSTP 
SPTRYSLSPS KSYKYSPKTP PRWAEDQNSL LKMICQQVEA IKKEMQELKL NSSNSASPHR 
WPTENYGPDS VPDGYQGSQT FHGAPLTVAT TGPSVYYSQS PAYNSQYLLR PAANVTPTKG 
PVYGMNRLPP QQHIYAYPQQ MHTPPVQSSS ACMFSQEMYG PPALRFESPA TGILSPRGDD 
YFNYNVQQTS TNPPLPEPGY FTKPPIAAHA SRSAESKTIE FGKTNFVQPM PGEGLRPSLP 
TQAHTTQPTP FKFNSNFKSN DGDFTFSSPQ VVTQPPPAAY SNSESLLGLL TSDKPLQGDG 
YSGAKPIPGG QTIGPRNTFN FGSKNVSGIS FTENMGSSQQ KNSGFRRSDD MFTFHGPGKS 
VFGTPTLETA NKNHETDGGS AHGDDDDDGP HFEPVVPLPD KIEVKTGEED EEEFFCNRAK 
LFRFDVESKE WKERGIGNVK ILRHKTSGKI RLLMRREQVL KICANHYISP DMKLTPNAGS 
DRSFVWHALD YADELPKPEQ LAIRFKTPEE AALFKCKFEE AQSILKAPGT NVAMASNQAV 
RIVKEPTSHD NKDICKSDAG NLNFEFQVAK KEGSWWHCNS CSLKNASTAK KCVSCQNLNP 
SNKELVGPPL AETVFTPKTS PENVQDRFAL VTPKKEGHWD CSICLVRNEP TVSRCIACQN 
TKSANKSGSS FVHQASFKFG QGDLPKPINS DFRSVFSTKE GQWDCSACLV QNEGSSTKCA 
ACQNPRKQSL PATSIPTPAS FKFGTSETSK TLKSGFEDMF AKKEGQWDCS SCLVRNEANA 
TRCVACQNPD KPSPSTSVPA PASFKFGTSE TSKAPKSGFE GMFTKKEGQW DCSVCLVRNE 
ASATKCIACQ NPGKQNQTTS AVSTPASSET SKAPKSGFEG MFTKKEGQWD CSVCLVRNEA 
SATKCIACQN PGKQNQTTSA VSTPASSETS KAPKSGFEGM FTKKEGQWDC SVCLVRNEAS 
ATKCIACQCP SKQNQTTAIS TPASSEISKA PKSGFEGMFI RKGQWDCSVC CVQNESSSLK 
CVACDASKPT HKPIAEAPSA FTLGSEMKLH DSSGSQVGTG FKSNFSEKAS KFGNTEQGFK 
FGHVDQENSP SFMFQGSSNT EFKSTKEGFS IPVSADGFKF GISEPGNQEK KSEKPLENGT 
GFQAQDISGQ KNGRGVIFGQ TSSTFTFADL AKSTSGEGFQ FGKKDPNFKG FSGAGEKLFS 
SQYGKMANKA NTSGDFEKDD DAYKTEDSDD IHFEPVVQMP EKVELVTGEE DEKVLYSQRV 
KLFRFDAEVS QWKERGLGNL KILKNEVNGK LRMLMRREQV LKVCANHWIT TTMNLKPLSG 
SDRAWMWLAS DFSDGDAKLE QLAAKFKTPE LAEEFKQKFE ECQRLLLDIP LQTPHKLVDT 
GRAAKLIQRA EEMKSGLKDF KTFLTNDQTK VTEEENKGSG TGAAGASDTT IKPNPENTGP 
TLEWDNYDLR EDALDDSVSS SSVHASPLAS SPVRKNLFRF GESTTGFNFS FKSALSPSKS 
PAKLNQSGTS VGTDEESDVT QEEERDGQYF EPVVPLPDLV EVSSGEENEQ VVFSHRAKLY 
RYDKDVGQWK ERGIGDIKIL QNYDNKQVRI VMRRDQVLKL CANHRITPDM TLQNMKGTER 
VWLWTACDFA DGERKVEHLA VRFKLQDVAD SFKKIFDEAK TAQEKDSLIT PHVSRSSTPR 
ESPCGKIAVA VLEETTRERT DVIQGDDVAD ATSEVEVSST SETTPKAVVS PPKFVFGSES 
VKSIFSSEKS KPFAFGNSSA TGSLFGFSFN APLKSNNSET SSVAQSGSES KVEPKKCELS 
KNSDIEQSSD SKVKNLFASF PTEESSINYT FKTPEKAKEK KKPEDSPSDD DVLIVYELTP 
TAEQKALATK LKLPPTFFCY KNRPDYVSEE EEDDEDFETA VKKLNGKLYL DGSEKCRPLE 
ENTADNEKEC IIVWEKKPTV EEKAKADTLK LPPTFFCGVC SDTDEDNGNG EDFQSELQKV 
QEAQKSQTEE ITSTTDSVYT GGTEVMVPSF CKSEEPDSIT KSISSPSVSS ETMDKPVDLS 
TRKEIDTDST SQGESKIVSF GFGSSTGLSF ADLASSNSGD FAFGSKDKNF QWANTGAAVF 
GTQSVGTQSA GKVGEDEDGS DEEVVHNEDI HFEPIVSLPE VEVKSGEEDE EILFKERAKL 
YRWDRDVSQW KERGVGDIKI LWHTMKNYYR ILMRRDQVFK VCANHVITKT MELKPLNVSN 
NALVWTASDY ADGEAKVEQL AVRFKTKEVA DCFKKTFEEC QQNLMKLQKG HVSLAAELSK 
ETNPVVFFDV CADGEPLGRI TMELFSNIVP RTAENFRALC TGEKGFGFKN SIFHRVIPDF 
VCQGGDITKH DGTGGQSIYG DKFEDENFDV KHTGPGLLSM ANQGQNTNNS QFVITLKKAE 
HLDFKHVVFG FVKDGMDTVK KIESFGSPKG SVCRRITITE CGQI

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: RANBP2

Associated with

Cells (max top 100)

Other Information

Nup358, a cytoplasmically exposed nucleoporin with peptide repeats, Ran-GTP binding sites, zinc fingers, a cyclophilin A homologous domain, and a leucine-rich region. PubMed ID: 7775481

A giant nucleopore protein that binds Ran/TC4. PubMed ID: 7603572

Generation and annotation of the DNA sequences of human chromosomes 2 and 4. PubMed ID: 15815621

The Ran/TC4 GTPase-binding domain: identification by expression cloning and characterization of a conserved sequence motif. PubMed ID: 7724562

The nucleoporin RanBP2 has SUMO1 E3 ligase activity. PubMed ID: 11792325

The SUMO E3 ligase RanBP2 promotes modification of the HDAC4 deacetylase. PubMed ID: 12032081

Tpr is localized within the nuclear basket of the pore complex and has a role in nuclear protein export. PubMed ID: 11839768

Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry. PubMed ID: 15144186

RanBP2/Nup358 provides a major binding site for NXF1-p15 dimers at the nuclear pore complex and functions in nuclear mRNA export. PubMed ID: 14729961

The RanBP2 SUMO E3 ligase is neither HECT- nor RING-type. PubMed ID: 15378033

Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. PubMed ID: 15388847

Unique binding interactions among Ubc9, SUMO and RanBP2 reveal a mechanism for SUMO paralog selection. PubMed ID: 15608651

A general approach for investigating enzymatic pathways and substrates for ubiquitin-like modifiers. PubMed ID: 16620772

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

Parkin ubiquitinates and promotes the degradation of RanBP2. PubMed ID: 16332688

A probability-based approach for high-throughput protein phosphorylation analysis and site localization. PubMed ID: 16964243

Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis. PubMed ID: 18220336

Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle. PubMed ID: 18691976

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Large-scale phosphoproteome analysis of human liver tissue by enrichment and fractionation of phosphopeptides with strong anion exchange chromatography. PubMed ID: 18318008

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

RanBP2 and SENP3 function in a mitotic SUMO2/3 conjugation-deconjugation cycle on Borealin. PubMed ID: 18946085

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

mRNA export from mammalian cell nuclei is dependent on GANP. PubMed ID: 20005110

Bicaudal D2, dynein, and kinesin-1 associate with nuclear pore complexes and regulate centrosome and nuclear positioning during mitotic entry. PubMed ID: 20386726

Structural and biochemical characterization of the human cyclophilin family of peptidyl-prolyl isomerases. PubMed ID: 20676357

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

The oncogene eIF4E reprograms the nuclear pore complex to promote mRNA export and oncogenic transformation. PubMed ID: 22902403

Beta-catenin inhibits promyelocytic leukemia protein tumor suppressor function in colorectal cancer cells. PubMed ID: 22155184

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569

Immunoaffinity enrichment and mass spectrometry analysis of protein methylation. PubMed ID: 24129315

Uncovering global SUMOylation signaling networks in a site-specific manner. PubMed ID: 25218447

Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli. PubMed ID: 25114211

SUMO-2 orchestrates chromatin modifiers in response to DNA damage. PubMed ID: 25772364

System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability. PubMed ID: 25755297

Site-specific mapping of the human SUMO proteome reveals co-modification with phosphorylation. PubMed ID: 28112733

Vpu modulates DNA repair to suppress innate sensing and hyper-integration of HIV-1. PubMed ID: 32690953

Structure of a Ran-binding domain complexed with Ran bound to a GTP analogue: implications for nuclear transport. PubMed ID: 10078529

Solution structure of the Ran-binding domain 2 of RanBP2 and its interaction with the C terminus of Ran. PubMed ID: 15826666

Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. PubMed ID: 15931224

Determinants of small ubiquitin-like modifier 1 (SUMO1) protein specificity, E3 ligase, and SUMO-RanGAP1 binding activities of nucleoporin RanBP2. PubMed ID: 22194619

Crystal structure of the N-terminal domain of Nup358/RanBP2. PubMed ID: 22959972

Structural and functional analysis of the C-terminal domain of Nup358/RanBP2. PubMed ID: 23353830

Infection-triggered familial or recurrent cases of acute necrotizing encephalopathy caused by mutations in a component of the nuclear pore, RANBP2. PubMed ID: 19118815

A translocation t(2;8)(q12;p11) fuses FGFR1 to a novel partner gene, RANBP2/NUP358, in a myeloproliferative/myelodysplastic neoplasm. PubMed ID: 23041776

RANBP2 mutation causing autosomal dominant acute necrotizing encephalopathy attenuates its interaction with COX11. PubMed ID: 34400285